A study of the export systems of the xylitol and 2-deoxyglucose futile cycles has focused on the oepration and regulation of a phosphohydrolase that cleaves xylitol-5-P and 2 deoxyglucose-6-P, respectively, prior to the expulsion of the free sugars. The enzyme hydrolyses a number of sugar phosphates, but is specific for (1) substrates phosphorylated at the terminal carbon position, (2) substrates with a D-erythro configuration and, (3) preferentially hydrolyzes those substrates that exist in a cyclical (pyranose or furanose) configuration. Enzyme activity is regulated by a membrane-associated component which can be removed from the membrane by extensive washing in high salt solutions. This regulatory mechanism accounts for the conservation of phosphorylated intermediates during the operation of the futile cycles and, more importantly, may be responsible for maintaining a balance between the intracellular levels of Pi and phosphorylated glycolytic intermediates under all conditions of growth. The lectin-like protein responsible for coaggregation between Capnocytophaga gingivalis (emended) and Actinomyces israelii that is found on the cell envelope of the former has been identified and partially characterized. Two dimensional electrophoresis and western blot analysis used in conjunction with specifically adsorbed antisera revealed that the lectin is a basic protein (pI=i8.4) with a molecular weight of 155KDa. The protein is located exclusively on the outer member of C. gingivalis. Progress on the identification characterization of lectins found on cells of Bacteroides loeschei 1295 and Capnocytophaga ochracea stain 25 that are reponsible for coaggregation with strains of Streoptococcus sanguis and Actinomyces israelii will be summarized in Dr. Paul Kolenbrander's report.